GTP[S] stimulates migration of electropermeabilized neutrophils via a pertussis toxin-sensitive G-protein.

ABSTRACT

Electropermeabilized neutrophils were used to study the role of G-proteins in neutrophil migration. Rabbit neutrophils, under specific conditions, retained their ability to migrate after electropermeabilization. Introduction of guanosine-5'-[3-thio] triphosphate (GTP[S]) into the cell interior stimulated random migration and enhanced migration activated by a suboptimal concentration of formyl-methionyl-leucyl-phenylalanine (fMet-Leu-Phe) (10(-11) M). GTP[S] had no effect on random migration by intact cells, or on migration of intact cells activated with a suboptimal concentration of fMet-Leu-Phe, indicating that the effect of GTP[S] was intracellular. The effects of GTP[S] were inhibited by pertussis toxin and by guanosine-5'-[2-thio] diphosphate (GDP beta S) indicating that a pertussis toxin-sensitive G-protein was involved. GTP stimulated random migration to the same extent as GTP[S], but had only a small effect on migration activated by a suboptimal concentration of fMet-Leu-Phe (10(-11) M). Several other nucleotides tested had no effect on random migration or migration activated with 10(-11) M fMet-Leu-Phe. The results show that neutrophil migration can be potentiated by direct activation of a pertussis toxin-sensitive G-protein, and the results obtained with GTP suggest that possibly more than one G-protein is involved in this process.